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| | <StructureSection load='7pdc' size='340' side='right'caption='[[7pdc]], [[Resolution|resolution]] 1.83Å' scene=''> | | <StructureSection load='7pdc' size='340' side='right'caption='[[7pdc]], [[Resolution|resolution]] 1.83Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7pdc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PDC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7pdc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PDC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMP, CAP18, FALL39, HSD26 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pdc OCA], [https://pdbe.org/7pdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pdc RCSB], [https://www.ebi.ac.uk/pdbsum/7pdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pdc ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pdc OCA], [https://pdbe.org/7pdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pdc RCSB], [https://www.ebi.ac.uk/pdbsum/7pdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pdc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CAMP_HUMAN CAMP_HUMAN]] Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.<ref>PMID:16637646</ref> <ref>PMID:18818205</ref>
| + | [https://www.uniprot.org/uniprot/CAMP_HUMAN CAMP_HUMAN] Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.<ref>PMID:16637646</ref> <ref>PMID:18818205</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sancho-Vaello, E]] | + | [[Category: Sancho-Vaello E]] |
| - | [[Category: Zeth, K]] | + | [[Category: Zeth K]] |
| - | [[Category: Antimicrobial peptide]]
| + | |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Ll-37]]
| + | |
| Structural highlights
Function
CAMP_HUMAN Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.[1] [2]
Publication Abstract from PubMed
The human cathelicidin LL-37 serves a critical role in the innate immune system defending bacterial infections. LL-37 can interact with molecules of the cell wall and perforate cytoplasmic membranes resulting in bacterial cell death. To test the interactions of LL-37 and bacterial cell wall components we crystallized LL-37 in the presence of detergents and obtained the structure of a narrow tetrameric channel with a strongly charged core. The formation of a tetramer was further studied by cross-linking in the presence of detergents and lipids. Using planar lipid membranes a small but defined conductivity of this channel could be demonstrated. Molecular dynamic simulations underline the stability of this channel in membranes and demonstrate pathways for the passage of water molecules. Time lapse studies of E. coli cells treated with LL-37 show membrane discontinuities in the outer membrane followed by cell wall damage and cell death. Collectively, our results open a venue to the understanding of a novel AMP killing mechanism and allows the rational design of LL-37 derivatives with enhanced bactericidal activity.
The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics.,Sancho-Vaello E, Gil-Carton D, Francois P, Bonetti EJ, Kreir M, Pothula KR, Kleinekathofer U, Zeth K Sci Rep. 2020 Oct 15;10(1):17356. doi: 10.1038/s41598-020-74401-5. PMID:33060695[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li X, Li Y, Han H, Miller DW, Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J Am Chem Soc. 2006 May 3;128(17):5776-85. PMID:16637646 doi:10.1021/ja0584875
- ↑ Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem. 2008 Nov 21;283(47):32637-43. Epub 2008 Sep 25. PMID:18818205 doi:10.1074/jbc.M805533200
- ↑ Sancho-Vaello E, Gil-Carton D, Francois P, Bonetti EJ, Kreir M, Pothula KR, Kleinekathofer U, Zeth K. The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics. Sci Rep. 2020 Oct 15;10(1):17356. doi: 10.1038/s41598-020-74401-5. PMID:33060695 doi:http://dx.doi.org/10.1038/s41598-020-74401-5
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